Proteolysis of insulin-like growth factors (IGF) and IGF binding proteins by cathepsin D

Various proteinases have been postulated to function in limited proteolysis of insulin-like growth factor binding proteins (IGFBPs) contributing to the regulation of IGF bioavailability. In this study, we report on the in vitro degradation of IGFs and IGFBPs by the purified acidic aspartylprotease c...

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Veröffentlicht in:	Endocrinology (Philadelphia) 1997-09, Vol.138 (9), p.3797-3803
Hauptverfasser:	Claussen, M, Kübler, B, Wendland, M, Neifer, K, Schmidt, B, Zapf, J, Braulke, T
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Binding Sites Cathepsin D - isolation & purification Cathepsin D - metabolism Glycosylation Humans Hydrogen-Ion Concentration Insulin-Like Growth Factor Binding Protein 1 - metabolism Insulin-Like Growth Factor Binding Protein 2 - metabolism Insulin-Like Growth Factor Binding Protein 3 - chemistry Insulin-Like Growth Factor Binding Protein 3 - metabolism Insulin-Like Growth Factor Binding Protein 4 - chemistry Insulin-Like Growth Factor Binding Protein 4 - metabolism Insulin-Like Growth Factor Binding Proteins - metabolism Insulin-Like Growth Factor I - metabolism Insulin-Like Growth Factor II - metabolism Liver - enzymology Mice Peptide Fragments - metabolism Recombinant Proteins Sequence Analysis
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